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Volumn 84, Issue 3, 2003, Pages 1909-1918

Primary folding dynamics of sperm whale apomyoglobin: Core formation

Author keywords

[No Author keywords available]

Indexed keywords

ACID; APOMYOGLOBIN; SODIUM CHLORIDE; SOLVENT; TRYPTOPHAN;

EID: 0037339476     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74999-6     Document Type: Article
Times cited : (26)

References (49)
  • 1
    • 0027254057 scopus 로고
    • The molten globule intermediate of apomyoglobin and the process of protein folding
    • Barrick, D., and R. L. Baldwin. 1993. The molten globule intermediate of apomyoglobin and the process of protein folding. Prot. Sci. 2:869-876.
    • (1993) Prot. Sci. , vol.2 , pp. 869-876
    • Barrick, D.1    Baldwin, R.L.2
  • 2
    • 0028235775 scopus 로고
    • Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin
    • Barrick, D., F. Hughson, and R. Baldwin. 1994. Molecular mechanisms of acid denaturation The role of histidine residues in the partial unfolding of apomyoglobin. J. Mol. Biol. 237:588-601.
    • (1994) J. Mol. Biol. , vol.237 , pp. 588-601
    • Barrick, D.1    Hughson, F.2    Baldwin, R.3
  • 4
    • 0016290132 scopus 로고
    • Intensities and other spectral parameters of infrared amide bands of polypeptides in the alpha-helical form
    • Chirgadze, Y. N., and E. V. Brazhnikov. 1974. Intensities and other spectral parameters of infrared amide bands of polypeptides in the alpha-helical form. Biopolymers. 13:1701-1712.
    • (1974) Biopolymers , vol.13 , pp. 1701-1712
    • Chirgadze, Y.N.1    Brazhnikov, E.V.2
  • 5
    • 0015904265 scopus 로고
    • Intensities and other spectral parameters of infrared amide bands of polypeptides in the β- and random forms
    • Chirgadze, Y. N., B. V. Shestopalov, and S. Y. Venyaminov. 1973. Intensities and other spectral parameters of infrared amide bands of polypeptides in the β- and random forms. Biopolymers. 12:1337-1351.
    • (1973) Biopolymers , vol.12 , pp. 1337-1351
    • Chirgadze, Y.N.1    Shestopalov, B.V.2    Venyaminov, S.Y.3
  • 6
    • 0000714183 scopus 로고
    • A comparison of the conformation of sperm whale metmyoglobin with that of apomyoglobin
    • Crumpton, M. J., and A. Polson. 1965. A comparison of the conformation of sperm whale metmyoglobin with that of apomyoglobin. J. Mol. Biol. 11:722-729.
    • (1965) J. Mol. Biol. , vol.11 , pp. 722-729
    • Crumpton, M.J.1    Polson, A.2
  • 8
    • 0031851978 scopus 로고    scopus 로고
    • Equilibrium NMR studies of unfolded and partially folded proteins
    • Dyson, H. J., and P. E. Wright. 1998. Equilibrium NMR studies of unfolded and partially folded proteins. Nat. Struc. Biol. NMR Suppl. 5:499-503.
    • (1998) Nat. Struc. Biol. NMR Suppl. , vol.5 , pp. 499-503
    • Dyson, H.J.1    Wright, P.E.2
  • 9
    • 0034696675 scopus 로고    scopus 로고
    • Native and nonnative secondary structure and dynamics in the pH 4 intermediate of apomyoglobin
    • Eliezer, D., J. Chung, H. J. Dyson, and P. E. Wright. 2000. Native and nonnative secondary structure and dynamics in the pH 4 intermediate of apomyoglobin. Biochemistry. 39:2894-2901.
    • (2000) Biochemistry , vol.39 , pp. 2894-2901
    • Eliezer, D.1    Chung, J.2    Dyson, H.J.3    Wright, P.E.4
  • 10
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer, D., and P. E. Wright. 1996. Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 263:531-538.
    • (1996) J. Mol. Biol. , vol.263 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 11
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer, D., J. Yao, H. J. Dyson, and P. E. Wright. 1998. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat. Struct. Biol. 5:148-155.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 14
    • 0032067753 scopus 로고    scopus 로고
    • The core of apomyoglobin folds at the diffusion limit
    • Gilmanshin, R., R. H. Callender, and R. B. Dyer. 1998. The core of apomyoglobin folds at the diffusion limit. Nat. Struct. Biol. 5:363-365.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 363-365
    • Gilmanshin, R.1    Callender, R.H.2    Dyer, R.B.3
  • 15
    • 0030866261 scopus 로고    scopus 로고
    • Structural heterogeneity of the various forms of apomyoglobin: Implications for protein folding
    • Gilmanshin, R., R. B. Dyer, and R. H. Callender. 1997. Structural heterogeneity of the various forms of apomyoglobin: implications for protein folding. Prot. Sci. 6:2134-2142.
    • (1997) Prot. Sci. , vol.6 , pp. 2134-2142
    • Gilmanshin, R.1    Dyer, R.B.2    Callender, R.H.3
  • 16
    • 0035340960 scopus 로고    scopus 로고
    • Structures of apomyoglobin's various acid-destabilized forms
    • Gilmanshin, R., M. Gulotta, R. B. Dyer, and R. H. Callender. 2001. Structures of apomyoglobin's various acid-destabilized forms. Biochemistry. 40:5127-5136.
    • (2001) Biochemistry , vol.40 , pp. 5127-5136
    • Gilmanshin, R.1    Gulotta, M.2    Dyer, R.B.3    Callender, R.H.4
  • 17
    • 0001196094 scopus 로고    scopus 로고
    • Study of the ribonuclease S-peptide/S-protein complex by means of Raman difference spectroscopy
    • Gilmanshin, R., J. Van Beek, and R. Callender. 1996. Study of the ribonuclease S-peptide/S-protein complex by means of Raman difference spectroscopy. J. Phys. Chem. 100:16754-16760.
    • (1996) J. Phys. Chem. , vol.100 , pp. 16754-16760
    • Gilmanshin, R.1    Van Beek, J.2    Callender, R.3
  • 18
    • 0030817794 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics and structure of the I-form of apomyoglobin
    • Gilmanshin, R., S. Williams, R. H. Callender, R. B. Dyer, and W. H. Woodruff. 1997. Fast events in protein folding: relaxation dynamics and structure of the I-form of apomyoglobin. Biochemistry. 36:15006-15012.
    • (1997) Biochemistry , vol.36 , pp. 15006-15012
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Dyer, R.B.4    Woodruff, W.H.5
  • 19
    • 0030963424 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin
    • Gilmanshin, R., S. Williams, R. H. Callender, W. Woodruff, and R. B. Dyer. 1997. Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci. USA. 94:3709-3713.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3709-3713
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.4    Dyer, R.B.5
  • 20
    • 0028329347 scopus 로고
    • Thermodynamic puzzle of apomyoglobin unfolding
    • Griko, Y. V., and P. L. Privalov. 1994. Thermodynamic puzzle of apomyoglobin unfolding. J. Mol. Biol. 235:1318-1325.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1318-1325
    • Griko, Y.V.1    Privalov, P.L.2
  • 22
    • 0035339911 scopus 로고    scopus 로고
    • Core formation in apomyoglobin: Probing the upper reaches of the folding energy landscape
    • Gulotta, M., R. Gilmanshin, R. H. Callender, and R. B. Dyer. 2001. Core formation in apomyoglobin: probing the upper reaches of the folding energy landscape. Biochemistry. 40:5137-5143.
    • (2001) Biochemistry , vol.40 , pp. 5137-5143
    • Gulotta, M.1    Gilmanshin, R.2    Callender, R.H.3    Dyer, R.B.4
  • 23
    • 0035793222 scopus 로고    scopus 로고
    • Rate of interchain contact formation in an unfolded protein: Temperature and denaturant effects
    • Hagen, S., C. Carswell, and E. Sjolander. 2001. Rate of interchain contact formation in an unfolded protein: temperature and denaturant effects. J. Mol. Biol. 305:1161-1171.
    • (2001) J. Mol. Biol. , vol.305 , pp. 1161-1171
    • Hagen, S.1    Carswell, C.2    Sjolander, E.3
  • 24
    • 0034714154 scopus 로고    scopus 로고
    • Two-state expansion and collapse of a polypeptide
    • Hagen, S., and W. Eaton. 2000. Two-state expansion and collapse of a polypeptide. J. Mol. Biol. 301:1019-1027.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1019-1027
    • Hagen, S.1    Eaton, W.2
  • 25
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • Haris, P. I., and D. Chapman. 1995. The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers. 37:251-263.
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 26
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson, F. M., P. E. Wright, and R. L. Baldwin. 1990. Structural characterization of a partly folded apomyoglobin intermediate. Science. 249:1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 28
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M., and H. H. Mantsch. 1995. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30:95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 29
    • 0032549072 scopus 로고    scopus 로고
    • Two forms of the pH 4 folding intermediate of apomyoglobin
    • Jamin, M., and R. Baldwin. 1998. Two forms of the pH 4 folding intermediate of apomyoglobin. J. Mol. Biol. 276:491-504.
    • (1998) J. Mol. Biol. , vol.276 , pp. 491-504
    • Jamin, M.1    Baldwin, R.2
  • 30
    • 0034691198 scopus 로고    scopus 로고
    • Measuring the rate of intramolecular contact formation in polypeptides
    • Lapidus, L., W. Eaton, and J. Hofrichter. 2000. Measuring the rate of intramolecular contact formation in polypeptides. Proc. Natl. Acad. Sci. USA. 97:7220-7225.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7220-7225
    • Lapidus, L.1    Eaton, W.2    Hofrichter, J.3
  • 31
    • 0030056766 scopus 로고    scopus 로고
    • The native state of apomyoglobin described by proton NMR spectroscopy: The A-B-G-H interface of wild-type sperm whale apomyoglobin
    • Lecomte, J. T., Y. H. Kao, and M. J. Cocco. 1996. The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin. Proteins. 25:267-285.
    • (1996) Proteins , vol.25 , pp. 267-285
    • Lecomte, J.T.1    Kao, Y.H.2    Cocco, M.J.3
  • 32
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh, S. N., M. S. Kay, and R. L. Baldwin. 1995. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl. Acad. Sci. USA. 92:5446-5450.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 33
    • 0025360593 scopus 로고
    • Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect
    • Makhatadze, G. I., and P. L. Privalov. 1990. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect. J. Mol. Biol. 213:375-384.
    • (1990) J. Mol. Biol. , vol.213 , pp. 375-384
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 34
    • 0034684214 scopus 로고    scopus 로고
    • Infrared spectra of amide groups in α-helical proteins: Evidence for hydrogen bonding between helices and water
    • Manas. E. S., Z. Getahun, W. W. Wright, W. F. DeGrado, and J. M. Vanderkooi. 2000. Infrared spectra of amide groups in α-helical proteins: evidence for hydrogen bonding between helices and water. J. Am. Chem. Soc. 122:9883-9890.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9883-9890
    • Manas, E.S.1    Getahun, Z.2    Wright, W.W.3    DeGrado, W.F.4    Vanderkooi, J.M.5
  • 35
    • 0029064280 scopus 로고
    • FTIR spectroscopy of alanine-based peptides: Assignment of the amide I′ modes for random coil and helix
    • Martinez, G., and G. Millhauser. 1995. FTIR spectroscopy of alanine-based peptides: assignment of the amide I′ modes for random coil and helix. J. Struct. Biol. 114:23-27.
    • (1995) J. Struct. Biol. , vol.114 , pp. 23-27
    • Martinez, G.1    Millhauser, G.2
  • 36
    • 0031940406 scopus 로고    scopus 로고
    • The early folding kinetics of apomyoglobin
    • Pappu, R. V., and D. L. Weaver. 1998. The early folding kinetics of apomyoglobin. Prot. Sci. 7:480-490.
    • (1998) Prot. Sci. , vol.7 , pp. 480-490
    • Pappu, R.V.1    Weaver, D.L.2
  • 37
    • 0025287103 scopus 로고
    • Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects
    • Privalov, P. L., and G. I. Makhatadze. 1990. Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects. J. Mol. Biol. 213:385-391.
    • (1990) J. Mol. Biol. , vol.213 , pp. 385-391
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 38
    • 0030062907 scopus 로고    scopus 로고
    • Infrared amide I′ band of the coiled coil
    • Reisdorf, W. C., Jr., and S. Krimm. 1996. Infrared amide I′ band of the coiled coil. Biochemistry. 35:1383-1386.
    • (1996) Biochemistry , vol.35 , pp. 1383-1386
    • Reisdorf W.C., Jr.1    Krimm, S.2
  • 39
    • 0030947929 scopus 로고    scopus 로고
    • Folding propensities of peptide fragments of myoglobin
    • Reymond, M. T., G. Merutka, H. J. Dyson, and P. E. Wright. 1997. Folding propensities of peptide fragments of myoglobin. Prot. Sci. 6:706-716.
    • (1997) Prot. Sci. , vol.6 , pp. 706-716
    • Reymond, M.T.1    Merutka, G.2    Dyson, H.J.3    Wright, P.E.4
  • 40
    • 0034282637 scopus 로고    scopus 로고
    • The stabilities of mammalian apomyoglobins vary over a 600-fold range and can be enhanced by comparative mutagenesis
    • Scott, E. E., E. V. Paster, and J. S. Olson. 2000. The stabilities of mammalian apomyoglobins vary over a 600-fold range and can be enhanced by comparative mutagenesis. J. Biol. Chem. 275:27129-27136.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27129-27136
    • Scott, E.E.1    Paster, E.V.2    Olson, J.S.3
  • 41
    • 0027248899 scopus 로고
    • Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin
    • Shin, H.-C., G. Merutka, J. P. Waltho, L. L. Tennant, H. J. Dyson, and P. E. Wright. 1993. Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin. Biochemistry 32:6356-6364.
    • (1993) Biochemistry , vol.32 , pp. 6356-6364
    • Shin, H.-C.1    Merutka, G.2    Waltho, J.P.3    Tennant, L.L.4    Dyson, H.J.5    Wright, P.E.6
  • 42
    • 0027165689 scopus 로고
    • Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal
    • Shin, H.-C., G. Merutka, J. P. Waltho, P. E. Wright, and H. J. Dyson. 1993. Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal. Biochemistry. 32:6348-6355.
    • (1993) Biochemistry , vol.32 , pp. 6348-6355
    • Shin, H.-C.1    Merutka, G.2    Waltho, J.P.3    Wright, P.E.4    Dyson, H.J.5
  • 43
    • 0023462496 scopus 로고
    • High-level expression of sperm whale myoglobin in Escherichia coli
    • Springer, B. A., and S. G. Sligar. 1987. High-level expression of sperm whale myoglobin in Escherichia coli. Proc. Natl. Acad. Sci. USA. 84:8961-8965.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8961-8965
    • Springer, B.A.1    Sligar, S.G.2
  • 44
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • Surewicz, W. K., and H. H. Mantsch. 1988. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta. 952:115-130.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 45
    • 36749116443 scopus 로고
    • First passage time approach to diffusion controlled reactions
    • Szabo, A., K. Schulten, and Z. Schulten. 1980. First passage time approach to diffusion controlled reactions. J. Chem. Phys. 72:4350-4357.
    • (1980) J. Chem. Phys. , vol.72 , pp. 4350-4357
    • Szabo, A.1    Schulten, K.2    Schulten, Z.3
  • 46
    • 0027165688 scopus 로고
    • Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G-helix and H-helix of myoglobin
    • Waltho, J. P., V. A. Feher, G. Merutka, H. J. Dyson, and P. E. Wright. 1993. Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G-helix and H-helix of myoglobin. Biochemistry. 32:6337-6347.
    • (1993) Biochemistry , vol.32 , pp. 6337-6347
    • Waltho, J.P.1    Feher, V.A.2    Merutka, G.3    Dyson, H.J.4    Wright, P.E.5
  • 48
    • 0038557941 scopus 로고    scopus 로고
    • Cavitation and heat transfer effects in laser-induced temperature-jump studies of protein dynamics
    • Wray, W., T. Aida, and R. Dyer. 2002. Cavitation and heat transfer effects in laser-induced temperature-jump studies of protein dynamics. Appl. Phys. B. 74:55-66.
    • (2002) Appl. Phys. B , vol.74 , pp. 55-66
    • Wray, W.1    Aida, T.2    Dyer, R.3
  • 49
    • 0035957221 scopus 로고    scopus 로고
    • NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding
    • Yao, J., J. Chung, D. Eliezer, P. E. Wright, and H. J. Dyson. 2001. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry. 40:3561-3571.
    • (2001) Biochemistry , vol.40 , pp. 3561-3571
    • Yao, J.1    Chung, J.2    Eliezer, D.3    Wright, P.E.4    Dyson, H.J.5


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